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Isolation of the biunctional enzyme lysine 2-oxoglutarate reductase-saccharopine dehydrogenase from Phaseolus vulgaris.

Lima, S. T. C. and Azevedo, R. A. and Santoro, L. G. and Gaziola, S. A. and Lea, P. J. (2003) Isolation of the biunctional enzyme lysine 2-oxoglutarate reductase-saccharopine dehydrogenase from Phaseolus vulgaris. Amino Acids, 24 (1-2). pp. 179-186. ISSN 0939-4451

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Abstract

Lysine is catabolyzed by the bifunctional enzyme lysine 2-oxoglutarate reductase-saccharopine dehydrogenase (LOR-SDH) in both animals and plants. LOR condenses lysine and 2-oxoglutarate into saccharopine, using NADPH as cofactor and SDH converts saccharopine into α-aminoadipate δ-semialdehyde and glutamic acid, using NAD as cofactor. The distribution pattern of LOR and SDH among different tissues of Phaseolus vulgaris was determined. The hypocotyl contained the highest specific activity, whereas in seeds the activities of LOR and SDH were below the limit of detection. Precipitation of hypocotyl proteins with increasing concentrations of PEG 8000 revealed one broad peak of SDH activity, indicating that two isoforms may be present, a bifunctional LOR-SDH and possibly a monofunctional SDH. During the purification of the hypocotyl enzyme, the LOR activity proved to be very unstable, following ion-exchange chromatography. Depending on the purification procedure, the protein eluted as a monomer of 91–94 kDa containing only SDH activity, or as a dimer of 190 kDa with both, LOR and SDH activities, eluting together.

Item Type: Article
Journal or Publication Title: Amino Acids
Uncontrolled Keywords: Phaseolus vulgaris - Catabolism - Lysine - Lysine 2-oxoglutarate reductase - Saccharopine dehydrogenase
Subjects: Q Science > QH Natural history > QH301 Biology
Departments: Faculty of Science and Technology > Lancaster Environment Centre
ID Code: 10708
Deposited By: Mr Richard Ingham
Deposited On: 23 Jul 2008 08:39
Refereed?: Yes
Published?: Published
Last Modified: 18 Sep 2013 15:56
Identification Number:
URI: http://eprints.lancs.ac.uk/id/eprint/10708

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